Identification of a putative target for Rho as the serine-threonine kinase protein kinase N

Mutsuki Amano, Hideyuki Mukai, Yoshitaka Ono, Kazuyasu Chihara, Takeshi Matsui, Yuko Hamajima, Katsuya Okawa, Akihiro Iwamatsu, Kozo Kaibuchi

Research output: Contribution to journalArticlepeer-review

387 Citations (Scopus)

Abstract

Rho, a Ras-like small guanosine triphosphatase, has been implicated in cytoskeletal responses to extracellular signals such as lysophosphatidic acid (LPA) to form stress fibers and focal contacts. The form of RhoA bound to guanosine triphosphate directly bound to and activated a serine-threonine kinase, protein kinase N (PKN). Activated RhoA formed a complex with PKN and activated it in COS-7 cells. PKN was phosphorylated in Swiss 3T3 cells stimulated with LPA, and this phosphorylation was blocked by treatment of cells with botulinum C3 exoenzyme. Activation of Rho may be linked directly to a serine-threonine kinase pathway.

Original languageEnglish
Pages (from-to)648-650
Number of pages3
JournalScience
Volume271
Issue number5249
DOIs
Publication statusPublished - 02-02-1996
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General

Fingerprint Dive into the research topics of 'Identification of a putative target for Rho as the serine-threonine kinase protein kinase N'. Together they form a unique fingerprint.

Cite this